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Foods 2017, 6(12), 108; https://doi.org/10.3390/foods6120108

Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis

1
Food Biosciences Department, Teagasc Food Research Centre, Ashtown, D15 Dublin, Ireland
2
School of Biological Sciences, College of Sciences and Health and Environment, Sustainability and Health Institute, DIT Kevin Street, D08 NF82 Dublin, Ireland
3
Food Chemistry and Technology Department, Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork P61 C996, Ireland
4
Food Quality and Sensory Science Department, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland
5
Parc Científic I Tecnològic Agroalimentari de Lleida, Parc de Gardeny, Edifici Fruit Centre, Institut de Recerca, Tecnològia Agroalimentàries (IRTA), 25003 Lleida, Spain
*
Author to whom correspondence should be addressed.
Received: 26 October 2017 / Revised: 23 November 2017 / Accepted: 27 November 2017 / Published: 4 December 2017
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides)
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Abstract

The renin-angiotensin-aldosterone system (RAAS) plays an important role in regulating hypertension by controlling vasoconstriction and intravascular fluid volume. RAAS itself is largely regulated by the actions of renin (EC 3.4.23.15) and the angiotensin-I-converting enzyme (ACE-I; EC 3.4.15.1). The enzyme dipeptidyl peptidase-IV (DPP-IV; EC 3.4.14.5) also plays a role in the development of type-2 diabetes. The inhibition of the renin, ACE-I, and DPP-IV enzymes has therefore become a key therapeutic target for the treatment of hypertension and diabetes. The aim of this study was to assess the bioactivity of different oat (Avena sativa) protein isolates and their ability to inhibit the renin, ACE-I, and DPP-IV enzymes. In silico analysis was carried out to predictthe likelihood of bioactive inhibitory peptides occurring from oat protein hydrolysates following in silico hydrolysis with the proteases papain and ficin. Nine peptides, including FFG, IFFFL, PFL, WWK, WCY, FPIL, CPA, FLLA, and FEPL were subsequently chemically synthesised, and their bioactivities were confirmed using in vitro bioassays. The isolated oat proteins derived from seven different oat varieties were found to inhibit the ACE-I enzyme by between 86.5 ± 10.7% and 96.5 ± 25.8%, renin by between 40.5 ± 21.5% and 70.9 ± 7.6%, and DPP-IV by between 3.7 ± 3.9% and 46.2 ± 28.8%. The activity of the synthesised peptides was also determined. View Full-Text
Keywords: oats; Avena sativa; bioactive peptides; ACE-I; renin; DPP-IV; renin-angiotensin-aldosterone system oats; Avena sativa; bioactive peptides; ACE-I; renin; DPP-IV; renin-angiotensin-aldosterone system
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Bleakley, S.; Hayes, M.; O’ Shea, N.; Gallagher, E.; Lafarga, T. Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis. Foods 2017, 6, 108.

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